Calcium in PDB 7k4w: Crystal Structure of Kemp Eliminase HG3.17 in the Inactive State

All present enzymatic activity of Crystal Structure of Kemp Eliminase HG3.17 in the Inactive State:
3.2.1.8;

The structure of Crystal Structure of Kemp Eliminase HG3.17 in the Inactive State, PDB code: 7k4w was solved by R.A.P.Padua, R.Otten, A.Bunzel, V.Nguyen, W.Pitsawong, M.Patterson, S.Sui, S.L.Perry, A.E.Cohen, D.Hilvert, D.Kern, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.04 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	61.390, 67.390, 74.700, 90.00, 90.00, 90.00
R / Rfree (%)	21 / 25.5

The binding sites of Calcium atom in the Crystal Structure of Kemp Eliminase HG3.17 in the Inactive State (pdb code 7k4w). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure of Kemp Eliminase HG3.17 in the Inactive State, PDB code: 7k4w:

Calcium binding site 1 out of 1 in the Crystal Structure of Kemp Eliminase HG3.17 in the Inactive State


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Kemp Eliminase HG3.17 in the Inactive State within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca401 b:27.4 occ:0.58 O A:HIS209 2.3 26.6 0.5 O A:HOH538 2.3 25.5 1.0 O A:HIS209 2.4 26.5 0.5 OE1 A:GLN214 2.4 22.8 1.0 O A:HOH622 2.4 28.3 1.0 O A:HOH597 2.4 27.3 1.0 O A:HOH579 2.5 26.3 1.0 HE22 A:GLN214 2.9 29.9 1.0 HG A:SER211 3.2 26.3 0.0 CD A:GLN214 3.2 22.6 1.0 H A:SER211 3.3 27.7 1.0 H A:SER211 3.4 27.5 0.0 NE2 A:GLN214 3.4 24.9 1.0 C A:HIS209 3.6 27.6 0.5 HA A:LEU210 3.6 30.0 1.0 C A:HIS209 3.6 27.6 0.5 HB2 A:HIS209 3.8 35.0 0.5 HB3 A:HIS209 3.8 35.0 0.5 HG A:SER211 3.9 25.9 1.0 OG A:SER211 4.0 21.9 0.0 OD1 A:ASN175 4.0 25.7 1.0 N A:SER211 4.1 23.0 1.0 N A:SER211 4.1 22.9 0.0 O A:HOH586 4.2 25.6 1.0 HE21 A:GLN214 4.2 29.9 1.0 CA A:LEU210 4.3 24.9 1.0 HB2 A:SER211 4.3 25.8 1.0 N A:LEU210 4.4 26.6 1.0 CB A:HIS209 4.5 29.1 0.5 OD2 A:ASP177 4.5 23.6 1.0 O A:HOH619 4.5 32.4 1.0 HH A:TYR181 4.5 29.7 1.0 HB3 A:HIS209 4.5 35.0 0.5 CA A:HIS209 4.6 29.1 0.5 C A:LEU210 4.6 25.3 1.0 CB A:HIS209 4.6 29.2 0.5 H A:HIS209 4.6 33.7 0.5 CA A:HIS209 4.6 29.0 0.5 HD23 A:LEU210 4.7 28.4 1.0 OG A:SER211 4.7 21.6 1.0 CG A:GLN214 4.7 20.5 1.0 H A:HIS209 4.7 33.7 0.5 ND1 A:HIS209 4.8 31.2 0.5 OD1 A:ASP177 4.9 20.9 1.0 HB3 A:SER211 4.9 25.9 0.0 CB A:SER211 4.9 21.5 1.0 CB A:SER211 4.9 21.6 0.0 HB3 A:GLN214 4.9 24.4 1.0 CG A:ASP177 5.0 22.9 1.0 HB2 A:GLN214 5.0 24.4 1.0 HG3 A:GLN214 5.0 24.6 1.0 N A:HIS209 5.0 28.1 0.5

R.Otten, R.A.P.Padua, H.A.Bunzel, V.Nguyen, W.Pitsawong, M.Patterson, S.Sui, S.L.Perry, A.E.Cohen, D.Hilvert, D.Kern. How Directed Evolution Reshapes the Energy Landscape in An Enzyme to Boost Catalysis. Science 2020.
ISSN: ESSN 1095-9203
PubMed: 33214289
DOI: 10.1126/SCIENCE.ABD3623